FTH1 Antibodies

Structure of FTH1

The molecular weight of the ferritin heavy chain subunit encoded by the FTH1 gene is approximately 21 kDa, and this molecular weight fluctuates slightly among different species due to minor differences in amino acid sequences.

This protein is composed of approximately 183 amino acids and forms a typical quaternary structure by folding its primary structure. The core function of FTH1 depends on the "iron oxidase" active center it forms, which contains multiple conserved histidine and glutamic acid residues and can catalyze the oxidation of divalent iron to trivalent iron and store it in the protein cavity. Its secondary structure is mainly composed of α -helices, which entangle with each other to form a hollow spherical structure, providing a site for the deposition of iron cores. A key feature is its possession of the "Ferroxidase" active site, which is not available in the light chain subunits. It is directly responsible for the rapid oxidation of iron ions and is crucial for the iron metabolism balance and antioxidant defense of cells.

Fig. 1 Schematic diagram illustrating oxidative stress response mediated by FTH1 downregulation in hESCs.¹

Key structural properties of FTH1:

• Conservative α -helical bundle tetramer structure
• Hydrophobic core constitute iron oxidase activity center
• Unique Ferroxidase loci ferrous iron oxidation

Functions of FTH1

The core function of the ferritin heavy chain encoded by the FTH1 gene is the storage and buffering of iron ions. It also participates in various cellular processes, including antioxidant defense and immune regulation.

Ferritin exhibits a synergistic binding to iron. Its spherical cavity structure allows for the storage of up to 4,500 iron atoms, making it an efficient and high-capacity intracellular iron buffering system, which is different from membrane proteins that directly transport iron.

Applications of FTH1 and FTH1 Antibody in Literature

1. Cui, Jingxuan, et al. "Protosappanin A protects DOX‐induced myocardial injury and cardiac dysfunction by targeting ACSL4/FTH1 axis‐dependent ferroptosis." Advanced Science 11.34 (2024): 2310227. https://doi.org/10.1002/advs.202310227

This study reports that protohematoxylin A effectively inhibits myocardial ferroptosis by targeting and binding to ACSL4 and FTH1, alleviates myocardial injury and dysfunction caused by doxorubicin, and provides a new therapeutic strategy for related cardiotoxic diseases.

2. Wang, Kun, et al. "Locally organised and activated Fth1hi neutrophils aggravate inflammation of acute lung injury in an IL-10-dependent manner." Nature Communications 13.1 (2022): 7703. https://doi.org/10.1038/s41467-022-35492-y

This study found through single-cell sequencing that in LPS-induced acute lung injury, there are two distinct neutrophil subpopulations with high expression of Fth1 and high expression of Prok2 in the lungs. Among them, the Fth1hi subgroup has stronger inflammatory and antioxidant properties. Its persistent retention will aggravate lung injury and may serve as a biomarker for the poor prognosis of ARDS.

3. Di Sanzo, Maddalena, et al. "FTH1 pseudogenes in cancer and cell metabolism." Cells 9.12 (2020): 2554. https://doi.org/10.3390/cells9122554

The article indicates that pseudogenes were once mistakenly regarded as "junk DNA", but in fact, they are defective copies of functional genes. Studies have shown that many pseudogenes play important biological roles through transcriptional regulatory mechanisms. This article focuses on reviewing the ferritin family, especially the possible functions and regulatory networks of its FTH1 pseudogene.

4. Dang, Yini, et al. "FTH1-and SAT1-induced astrocytic ferroptosis is involved in Alzheimer's disease: evidence from single-cell transcriptomic analysis." Pharmaceuticals 15.10 (2022): 1177. https://doi.org/10.3390/ph15101177

The article indicates that through single-cell sequencing analysis, it was found that astrocytes in the entorhinal cortex of patients with Alzheimer's disease decreased and the ferroptosis pathway was activated. FTH1 and SAT1 have been identified as key molecules regulating ferroptosis in astrocytes, which may be associated with emotional and cognitive impairment in AD, providing new targets for treatment.

5. Zhang, Luxia, et al. "Genome-Wide Identification and Functional Differentiation of the FTH1 Gene Family: Insights into Immune Response to Vibrio in the Blood Clam Anadara granosa." Fishes 10.12 (2025): 646. https://doi.org/10.3390/fishes10120646

The article indicates that seven FTH1 homologous genes have been identified in the genome of the clam. Among them, five contain conserved domains, whose expression is downregulated after Vibrio infection, which may be related to ferroptosi-like pathogen clearance. The remaining gene structures are atypical, and it is speculated that they are involved in non-classical functions such as vesicle transport.

Creative Biolabs: FTH1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality FTH1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom FTH1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our FTH1 antibodies, custom preparations, or technical support, contact us at email.